Structural Basis for a Novel Interaction between the NS1 Protein Derived from the 1918 Influenza Virus and RIG-I

Academic Article

Abstract

  • © 2015 Elsevier Ltd. Summary The influenza non-structural protein 1 (NS1) plays a critical role in antagonizing the innate immune response to infection. One interaction that facilitates this function is between NS1 and RIG-I, one of the main sensors of influenza virus infection. While NS1 and RIG-I are known to interact, it is currently unclear whether this interaction is direct or if it is mediated by other biomolecules. Here we demonstrate a direct, strain-dependent interaction between the NS1 RNA binding domain (NS1RBD) of the influenza A/Brevig Mission/1918 H1N1 (1918H1N1) virus and the second caspase activation and recruitment domain of RIG-I. Solving the solution structure of the 1918H1N1 NS1RBD revealed features in a functionally novel region that may facilitate the observed interaction. The biophysical and structural data herein suggest a possible mechanism by which strain-specific differences in NS1 modulate influenza virulence.
  • Published In

  • Structure  Journal
  • Digital Object Identifier (doi)

    Author List

  • Jureka AS; Kleinpeter AB; Cornilescu G; Cornilescu CC; Petit CM
  • Start Page

  • 2001
  • End Page

  • 2010
  • Volume

  • 23
  • Issue

  • 11